Latest update: September 24, 2018


ProGT37 (Gtf1)

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ProGT ID ProGT37 (Gtf1)
ProGT Pathway
Organism Information
Organism NameStreptococcus parasanguinis
Clinical ImplicationPathogenic
DomainBacteria
PhylumFirmicutes
ClassificationFamily: Streptococcaceae
Order: Lactobacillales
Class: Bacilli (or Firmibacteria)
Division or phylum: "Firmicutes"
Taxonomic ID (NCBI)1318
Genome Information
Gene BankDQ990875
EMBLDQ990875
Gene Information
Gene Namegtf1
Protein information
Protein NameGtf1 
UniProtKB/ SwissProt IDA1C3L9
NCBI Ref SeqWP_014713989.1.
UniProtKB Sequence>sp|A1C3L9|GTF1_STRPA Glycosyltransferase Gtf1 OS=Streptococcus parasanguinis GN=gtf1 PE=1 SV=1 MTIYNINLGIGWASSGVEYAQAYRAQILRSLGMPAKFIFTNMFQSENLEHFTKNIGFEDN EIIWLYGYFTDVKISGTTYKKDDLEATFSQCPTKKEASSDRKLIRYYFENQELYINASLY GENQEYVQRVEYVVKGKLIRKDYYSYTKVFSEFYSPGENGVQLCNRSFYNEDGSIAYEEI LSNEKSTFVFSNKICYGLEELLEFMLEDLSLTKSDLILLDRATGIGQVVFENIGAAKLAV VIHAEHFNEKNTDEHNILWNNYYEYQFTNADKVNAFITSTERQKILLEEQFTQYTSLHPK IVAIPVGSLDQLKFPEQSRKSFSMMTGSRLAIEKHIDWLIEGVALAQKRLPELTFDIYGE GGERRKLTELLTKLHAGEFIELKGHKQLDEIYQNYELYLTASTSEGFGLTLMEAVGSGLP IIGFDVPYGNQTFVCSGENGLLIERPKGDDRSRIVQAFADSIYEYFTKFKMADAQQYSYN IAENYKHEKLVERWKDFIEEMLND
EMBL CDSABL74004.1
Sequence length504 AA
Subcellular LocationMembrane (Integral component of membrane)
Function in Native Organism 1) The complex of two GTs namely Gtf1 and Gtf2 initiates the glycosylation of by transferring the GlcNAc to Fap 1 protein.
Potential Application1) Studying biosynthetic pathways and the enzymes involved in biofilm formation may help to design of new potential therapeutics to control bacterial biofilm formation in future.
Additional Information1) The N-terminal domain of Gtf1 directly interacts with Gtf2 and this interaction plays a critical role in Fap1 glycosylation.
Glycosyltransferase Information
Glycosylation TypeO- (Ser/Thr) linked 
CAZY FamilyGT4
EC Number (BRENDA)2.4.1.-
Mechanism of Glycan TransferSequential
Donor TypeNucleotide activated sugars
Donor SpecificityUDP-GlcNAc
Accessory GT IDProGT37.1ProGT37.2
Glycan Information
Glycan transferredMonosaccharide (GlcNAc) 
Method of Glycan IndentificationGC-MS
Experimental_strategiesIn vitro and In vivo  
Acceptor Subtrate Information
Acceptor Substrate name Fap1
ProGPdb ID ProGP209
Litrature
Year Of Validation2010 
Reference Zhou, M., Zhu, F., Dong, S., Pritchard, D., & Wu, H. (2010). A novel glucosyltransferase is required for glycosylation of a serine-rich adhesin and biofilm formation by Streptococcus parasanguinis. Journal of Biological Chemistry, jbc-M109.

Authors Zhou, M., Zhu, F., Dong, S., Pritchard, D., & Wu, H.
Research groupsDepartment of Pediatric Dentistry, University of Alabama at Birmingham, Birmingham, Alabama 35244, USA
Corresponding Author Wu, H.
ContactsDepartment of Pediatric Dentistry, University of Alabama at Birmingham, Birmingham, Alabama 35244, USA
Reference Zhu, F., Zhang, H., Yang, T., Haslam, S. M., Dell, A., & Wu, H. (2016). Engineering and dissecting the glycosylation pathway of a streptococcal serine-rich repeat adhesin. Journal of Biological Chemistry, jbc-M116.

Authors Zhu, F., Zhang, H., Yang, T., Haslam, S. M., Dell, A., & Wu, H.
Research groupsUniversity of Alabama at Birmingham, United States
Corresponding Author Wu, H.
ContactsUniversity of Alabama at Birmingham, United States
Reference Zhang, H., Zhou, M., Yang, T., Haslam, S. M., Dell, A., & Wu, H. (2016). A new helical binding domain mediates a unique glycosyltransferase activity of a bifunctional protein. Journal of Biological Chemistry, jbc-M116.

Authors Zhang, H., Zhou, M., Yang, T., Haslam, S. M., Dell, A., & Wu, H.
Research groupsUniversity of Alabama at Birmingham, United States
Corresponding Author Wu, H.
ContactsUniversity of Alabama at Birmingham, United States